ArticleNature2010
Structural changes of envelope proteins during alphavirus fusion.
Article in Nature, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 212 papers.
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Who cites it
212 citing papers in PubMed, 317 citations in OpenAlex.
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- Research progress on the role of host factors in Chikungunya virus infection and intervention strategies.Virulence · 2026Review
- Encephalitic alphavirus infection induces long-term humoral and cell-mediated responses in seropositive participants from Panama.PLoS neglected tropical diseases · 2026Article
- Recent progress in anti-Chikungunya virus drug discovery: Focus on the viral life cycle and direct-acting antivirals.Virologica Sinica · 2026Review
- Double functionalized Sindbis E2 glycoprotein modifies Sindbis tropism favouring infection of α5β1⁺ glioblastoma cells.Scientific reports · 2026Article
- Structural and immunogenic characterisation of ChAdOx1 Chik-derived Chikungunya VLPs supports a mechanistic rationale for vaccine-induced protection.Npj viruses · 2026Article
- Current status on encephalitic alphavirus vaccines development: Advances, challenges, and global health perspectives.Infectious medicine · 2026Review
- Asymmetric structural transitions in the icosahedral organization of Eastern equine encephalitis virus.Nature communications · 2026Article
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- Exosome-enriched extracellular vesicles are associated with Getah virus RNA and transmission-related readoutsFrontiers in cellular and infection microbiology · 2026Article
- Chikungunya Virus in 2025: Epidemiology, Immunopathogenesis, and Vaccine Development - A Narrative Review.Infection and drug resistance · 2026Review
- Molecular basis of ApoER2-mediated Semliki Forest virus entry.Nature communications · 2025Article
- Genomic characterization and evolutionary analysis of Chikungunya virus strains in Guangzhou, China, 2025.Virology journal · 2025Article
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- Structural insights into VLDLR recognition by western equine encephalitis virus.Nature communications · 2025Article
- Neutralizing antibodies against Chikungunya virus and structural elucidation of their mechanism of action.Nature communications · 2025Article
- A Review of the Biology of Chikungunya Virus Highlighting the Development of Current Novel Therapeutic and Prevention Approaches.Pathogens (Basel, Switzerland) · 2025Review
- ARRDC1 inhibits the replication of Semliki Forest virus by regulating the ubiquitination and degradation of viral nsP4.Journal of virology · 2025Article
- Structural and Functional Hallmarks of Sindbis Virus Proteins: From Virion Architecture to Pathogenesis.International journal of molecular sciences · 2025Review
- Determinants of human versus mosquito cell entry by the Chikungunya virus envelope proteins.bioRxiv : the preprint server for biology · 2025Article
152 more citing papers are in PubMed but not listed here.
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Authors and funding
5 authors at 2 institutions in 1 country.
Funding
Abstract
Alphaviruses are enveloped RNA viruses that have a diameter of about 700 Å and can be lethal human pathogens. Entry of virus into host cells by endocytosis is controlled by two envelope glycoproteins, E1 and E2. The E2-E1 heterodimers form 80 trimeric spikes on the icosahedral virus surface, 60 with quasi-three-fold symmetry and 20 coincident with the icosahedral three-fold axes arranged with T = 4 quasi-symmetry. The E1 glycoprotein has a hydrophobic fusion loop at one end and is responsible for membrane fusion. The E2 protein is responsible for receptor binding and protects the fusion loop at neutral pH. The lower pH in the endosome induces the virions to undergo an irreversible conformational change in which E2 and E1 dissociate and E1 forms homotrimers, triggering fusion of the viral membrane with the endosomal membrane and then releasing the viral genome into the cytoplasm. Here we report the structure of an alphavirus spike, crystallized at low pH, representing an intermediate in the fusion process and clarifying the maturation process. The trimer of E2-E1 in the crystal structure is similar to the spikes in the neutral pH virus except that the E2 middle region is disordered, exposing the fusion loop. The amino- and carboxy-terminal domains of E2 each form immunoglobulin-like folds, consistent with the receptor attachment properties of E2.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.